Ghendon Y Z, Markushin S G, Klimov A I, Lotte V D, Ginzburg V P
J Gen Virol. 1983 Feb;64 (Pt 2):291-304. doi: 10.1099/0022-1317-64-2-291.
A fowl plague virus (FPV) temperature-sensitive mutant, ts 303/1 having a ts mutation in gene 7 coding for the matrix (M) protein has been obtained. The mutant induced synthesis of virus-specific RNA and polypeptides as well as ribonuclear protein (RNP) formation in cells under non-permissive conditions; however, haemagglutinin cleavage was reduced, functionally active haemagglutinin and neuraminidase were absent and virions were not formed. In mutant-infected cells at 36 degrees C haemagglutinin cleavage was also reduced and virions formed had an altered NP:M ratio as well as a decreased haemagglutinin content. A population of virions formed under these conditions was heterogeneous both in morphology and in buoyant density. The data obtained suggest that a mutation in the M proteins of orthomyxoviruses can affect processing of the haemagglutinin and impair final stages of virion morphogenesis.
已获得一种禽瘟病毒（FPV）温度敏感突变体ts 303/1，其在编码基质（M）蛋白的基因7中存在温度敏感（ts）突变。该突变体在非允许条件下能诱导细胞中病毒特异性RNA和多肽的合成以及核糖核蛋白（RNP）的形成；然而，血凝素裂解减少，缺乏功能活性的血凝素和神经氨酸酶，且未形成病毒粒子。在36℃感染突变体的细胞中，血凝素裂解也减少，形成的病毒粒子的核蛋白（NP）与基质蛋白（M）的比例改变，血凝素含量降低。在这些条件下形成的一群病毒粒子在形态和浮力密度上均具有异质性。所获得的数据表明，正粘病毒M蛋白的突变可影响血凝素的加工，并损害病毒粒子形态发生的最后阶段。
